ID W5KCM2_ASTMX Unreviewed; 855 AA.
AC W5KCM2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Si:cabz01100188.1 {ECO:0000313|Ensembl:ENSAMXP00000005333.2};
GN Name=LOXL4 {ECO:0000313|Ensembl:ENSAMXP00000005333.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000005333.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000005333.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SIMILARITY: Belongs to the lysyl oxidase family.
CC {ECO:0000256|ARBA:ARBA00007492}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR AlphaFoldDB; W5KCM2; -.
DR STRING; 7994.ENSAMXP00000005333; -.
DR Ensembl; ENSAMXT00000005333.2; ENSAMXP00000005333.2; ENSAMXG00000005173.2.
DR eggNOG; ENOG502QSX8; Eukaryota.
DR GeneTree; ENSGT00940000157042; -.
DR HOGENOM; CLU_002555_3_0_1; -.
DR InParanoid; W5KCM2; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000005173; Expressed in bone element and 3 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.10.250.10; SRCR-like domain; 4.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR45817:SF5; LYSYL OXIDASE HOMOLOG 4; 1.
DR PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR Pfam; PF00530; SRCR; 4.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 4.
DR SUPFAM; SSF56487; SRCR-like; 4.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 4.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; LTQ {ECO:0000256|ARBA:ARBA00022477};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..855
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017181321"
FT DOMAIN 25..125
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 281..399
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 419..519
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 520..628
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 170..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 50..114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 63..124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 94..104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 365..375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 444..508
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 457..518
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 488..498
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 596..606
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 855 AA; 95157 MW; 4103924942B2AC32 CRC64;
MLTIPLAFCI LLLPVVAAIP PGFQVRLVGG RTSYEGRLEV FYNGAWGTVC DDEVTINLAN
VVCRELGYAR GLTWAHSAKF GEGQGPIWLD NVLCTGIENS VSDCRSNGWG VSDCTHGEDL
GIVCSPDSPQ QGHVPRYVEI TQPVVTPARP PETFRTTISA STRRGHEIAL NRNTQRGSPA
LPQLSGHQIQ LRRNTSPRRQ ENSVPRGHQL PGHLRNGAAY RRNQDIPPRP VAQSAQHIPE
PSTYERPLPV PVSRPEPSYQ EVENGSDVKK DLEDVRLRPV LPSTRGSAMV TEGVVEVRHA
GRWRHVCSLG WDLSSSRVVC GMLGYPAAEQ HKEHLYKKQW DSKMEDPAMR ALVSKKGYWV
ERVQCSGTET SLSQCQAQLS IPRNDASCIG GIYAVVRCVP GPQCHDAGSA PAAFFRYVVR
LKSGPRLGEG RVEVLREGKW GTVCDHLWDI TAASVVCREL GFGSAKEALR GAHMGQGTGP
IHMNSVQCTG RERSVLQCKY QEVPLRTCKH AQDVSVRCNV RLAGGREAAE GRVEVLMEVG
GVQRWGSVCS ENWGINEAMV VCRQLGFGFA SRAHQETWFW PGNRDAEEVI LSGTHCIGME
MSIQQCRKNG QVYCPRGGGG KAAGVTCVDI APDLVVDAQL VQETAYLEDR PLHLLTCAHE
ENCLSSSAAR MNWPYGHRRL LRFSSRIMNL GRADFRPRAS RDAWVWHQCH RHYHSIEVFT
HYDLLTMNGT KVAEGHKASF CLEDTYCPEG LSKRYACYNM GEQGISVGCW DTYRHDIDCQ
WVDITDVRPG DYIFQVEVNP SLDMAESDFQ NNVVRCRCRY DGGRVYLYGC HAGDAYSAEV
EDLFEHQRQI SNNFL
//
